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Conserved domains on  [gi|491001101|ref|WP_004862823|]
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MULTISPECIES: diaminopropionate ammonia-lyase [Raoultella]

Protein Classification

PALP domain-containing protein( domain architecture ID 751)

PALP domain-containing protein belonging to the tryptophan synthase beta superfamily (fold type II) that consists of pyridoxal phosphate (PLP)-dependent enzymes that catalyze beta-replacement and beta-elimination reactions

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Trp-synth-beta_II super family cl00342
Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP) ...
 5-393 0e+00

Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP)-dependent enzymes catalyzes beta-replacement and beta-elimination reactions. This CD corresponds to aminocyclopropane-1-carboxylate deaminase (ACCD), tryptophan synthase beta chain (Trp-synth_B), cystathionine beta-synthase (CBS), O-acetylserine sulfhydrylase (CS), serine dehydratase (Ser-dehyd), threonine dehydratase (Thr-dehyd), diaminopropionate ammonia lyase (DAL), and threonine synthase (Thr-synth). ACCD catalyzes the conversion of 1-aminocyclopropane-1-carboxylate to alpha-ketobutyrate and ammonia. Tryptophan synthase folds into a tetramer, where the beta chain is the catalytic PLP-binding subunit and catalyzes the formation of L-tryptophan from indole and L-serine. CBS is a tetrameric hemeprotein that catalyzes condensation of serine and homocysteine to cystathionine. CS is a homodimer that catalyzes the formation of L-cysteine from O-acetyl-L-serine. Ser-dehyd catalyzes the conversion of L- or D-serine to pyruvate and ammonia. Thr-dehyd is active as a homodimer and catalyzes the conversion of L-threonine to 2-oxobutanoate and ammonia. DAL is also a homodimer and catalyzes the alpha, beta-elimination reaction of both L- and D-alpha, beta-diaminopropionate to form pyruvate and ammonia. Thr-synth catalyzes the formation of threonine and inorganic phosphate from O-phosphohomoserine.


The actual alignment was detected with superfamily member TIGR03528:

Pssm-ID: 444852  Cd Length: 396  Bit Score: 702.63  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491001101    5 SLKMDIAENRF-FTGETSPLFSRQQAQQARHFHQKIVGYKPTPLYALKSLAALFGVSTILVKDESQRFGLNAFKMLGGAY 83
Cdd:TIGR03528   1 SIKIIINDNKKaTNGTDLSLLSKEEAEKVRAFHQSFPGYQPTPLAELDNLAKHLGVGSILVKDESYRFGLNAFKVLGGSY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491001101   84 AIAQLLCEKYHLDINAFSFATFKSS-IKEKM---TFATTTDGNHGRGVAWAAQQLGQNAVIYMPKGSAQERVDAILRLGA 159
Cdd:TIGR03528  81 AIGKYLAEKLGKDISELSFEKLKSNeIREKLgdiTFVTATDGNHGRGVAWAANQLGQKSVVYMPKGSAQERLENIRAEGA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491001101  160 RCIVTEMNYDDTVRFTMQTARQNGWEVVQDTAWEGYTKIPTWIMQGYATLADEAVEQMAAMGIARPTHVFLQAGVGAMAG 239
Cdd:TIGR03528 161 ECTITDLNYDDAVRLAWKMAQENGWVMVQDTAWEGYEKIPTWIMQGYGTLALEALEQLKEQGVEKPTHVFLQAGVGSFAG 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491001101  240 GVLGYLVDVFGARDLHSVIVEPELADCLYRSGVK--GQIVNVGGSMATIMAGLACGEPNPLGWDILRNCATQFISCQDAV 317
Cdd:TIGR03528 241 AVQGYFASVYGEERPITVIVEPDKADCIYRSAIAddGKPHFVTGDMATIMAGLACGEPNTIGWEILRDYASQFISCPDWV 320

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491001101  318 AALGMRVLGNPLGTDPRVISGESGAVGLGILSAVHFHPQREALMNKLGLDSRSVVLVISTEGDTDVEHYREVVWEG 393
Cdd:TIGR03528 321 AAKGMRILGNPLKGDPRVISGESGAVGTGLLAAVMTHPDYKELREKLQLDKNSRVLLISTEGDTDPDHYRKIVWNG 396
 
Name Accession Description Interval E-value
2_3_DAP_am_ly TIGR03528
diaminopropionate ammonia-lyase; Members of this protein family are the homodimeric, pyridoxal ...
 5-393 0e+00

diaminopropionate ammonia-lyase; Members of this protein family are the homodimeric, pyridoxal phosphate enzyme diaminopropionate ammonia-lyase, which adds water to remove two amino groups, leaving pyruvate.


Pssm-ID: 274631  Cd Length: 396  Bit Score: 702.63  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491001101    5 SLKMDIAENRF-FTGETSPLFSRQQAQQARHFHQKIVGYKPTPLYALKSLAALFGVSTILVKDESQRFGLNAFKMLGGAY 83
Cdd:TIGR03528   1 SIKIIINDNKKaTNGTDLSLLSKEEAEKVRAFHQSFPGYQPTPLAELDNLAKHLGVGSILVKDESYRFGLNAFKVLGGSY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491001101   84 AIAQLLCEKYHLDINAFSFATFKSS-IKEKM---TFATTTDGNHGRGVAWAAQQLGQNAVIYMPKGSAQERVDAILRLGA 159
Cdd:TIGR03528  81 AIGKYLAEKLGKDISELSFEKLKSNeIREKLgdiTFVTATDGNHGRGVAWAANQLGQKSVVYMPKGSAQERLENIRAEGA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491001101  160 RCIVTEMNYDDTVRFTMQTARQNGWEVVQDTAWEGYTKIPTWIMQGYATLADEAVEQMAAMGIARPTHVFLQAGVGAMAG 239
Cdd:TIGR03528 161 ECTITDLNYDDAVRLAWKMAQENGWVMVQDTAWEGYEKIPTWIMQGYGTLALEALEQLKEQGVEKPTHVFLQAGVGSFAG 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491001101  240 GVLGYLVDVFGARDLHSVIVEPELADCLYRSGVK--GQIVNVGGSMATIMAGLACGEPNPLGWDILRNCATQFISCQDAV 317
Cdd:TIGR03528 241 AVQGYFASVYGEERPITVIVEPDKADCIYRSAIAddGKPHFVTGDMATIMAGLACGEPNTIGWEILRDYASQFISCPDWV 320

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491001101  318 AALGMRVLGNPLGTDPRVISGESGAVGLGILSAVHFHPQREALMNKLGLDSRSVVLVISTEGDTDVEHYREVVWEG 393
Cdd:TIGR03528 321 AAKGMRILGNPLKGDPRVISGESGAVGTGLLAAVMTHPDYKELREKLQLDKNSRVLLISTEGDTDPDHYRKIVWNG 396
PRK08206 PRK08206
diaminopropionate ammonia-lyase; Provisional
 1-396 0e+00

diaminopropionate ammonia-lyase; Provisional


Pssm-ID: 236186  Cd Length: 399  Bit Score: 681.99  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491001101   1 MSAFSLKMDIAENRFFTGETSPLFSRQQAQQARHFHQKIVGYKPTPLYALKSLAALFGVSTILVKDESQRFGLNAFKMLG 80
Cdd:PRK08206   1 MSMFLLKNNIADNKPYDGADLPLLSQEEAKKARAFHQSFPGYAPTPLVALPDLAAELGVGSILVKDESYRFGLNAFKALG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491001101  81 GAYAIAQLLCEKYHLDINAFSFATFKS----SIKEKMTFATTTDGNHGRGVAWAAQQLGQNAVIYMPKGSAQERVDAILR 156
Cdd:PRK08206  81 GAYAVARLLAEKLGLDISELSFEELTSgevrEKLGDITFATATDGNHGRGVAWAAQQLGQKAVIYMPKGSSEERVDAIRA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491001101 157 LGARCIVTEMNYDDTVRFTMQTARQNGWEVVQDTAWEGYTKIPTWIMQGYATLADEAVEQMAAMGiARPTHVFLQAGVGA 236
Cdd:PRK08206 161 LGAECIITDGNYDDSVRLAAQEAQENGWVVVQDTAWEGYEEIPTWIMQGYGTMADEAVEQLKEMG-VPPTHVFLQAGVGS 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491001101 237 MAGGVLGYLVDVFGARDLHSVIVEPELADCLYRSGVKGQIVNVGGSMATIMAGLACGEPNPLGWDILRNCATQFISCQDA 316
Cdd:PRK08206 240 LAGAVLGYFAEVYGEQRPHFVVVEPDQADCLYQSAVDGKPVAVTGDMDTIMAGLACGEPNPLAWEILRNCADAFISCPDE 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491001101 317 VAALGMRVLGNPLGTDPRVISGESGAVGLGILSAVHFHPQREALMNKLGLDSRSVVLVISTEGDTDVEHYREVVWEGKYP 396
Cdd:PRK08206 320 VAALGMRILANPLGGDPPIVSGESGAVGLGALAALMTDPDYQELREKLGLDEDSRVLLISTEGDTDPDRYREIVWEGKYA 399
IlvA COG1171
Threonine deaminase [Amino acid transport and metabolism]; Threonine deaminase is part of the ...
 20-393 3.14e-93

Threonine deaminase [Amino acid transport and metabolism]; Threonine deaminase is part of the Pathway/BioSystem: Isoleucine, leucine, valine biosynthesis


Pssm-ID: 440784 [Multi-domain]  Cd Length: 327  Bit Score: 282.70  E-value: 3.14e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491001101  20 TSPLFSRQQAQQARHFHQKIVgyKPTPLYALKSLAALFGvSTILVKDESQRFgLNAFKMLGGAYAIAQLlcekyhldina 99
Cdd:COG1171    2 TALMPTLADIEAAAARIAGVV--RRTPLLRSPTLSERLG-AEVYLKLENLQP-TGSFKLRGAYNALASL----------- 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491001101 100 fsfatfkSSIKEKMTFATTTDGNHGRGVAWAAQQLGQNAVIYMPKGSAQERVDAILRLGARCIVTEMNYDDTVRFTMQTA 179
Cdd:COG1171   67 -------SEEERARGVVAASAGNHAQGVAYAARLLGIPATIVMPETAPAVKVAATRAYGAEVVLHGDTYDDAEAAAAELA 139

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491001101 180 RQNGWEVVQDTAwegytkiPTWIMQGYATLADEAVEQMAAmgiarPTHVFLQAGVGAMAGGVLGYLVDVfgARDLHSVIV 259
Cdd:COG1171  140 EEEGATFVHPFD-------DPDVIAGQGTIALEILEQLPD-----LDAVFVPVGGGGLIAGVAAALKAL--SPDIRVIGV 205

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491001101 260 EPELADCLYRSGVKGQIVNVGGsMATIMAGLACGEPNPLGWDILRNCATQFISCQDAVAALGMRVLGNPLgtdpRVISGE 339
Cdd:COG1171  206 EPEGAAAMYRSLAAGEPVTLPG-VDTIADGLAVGRPGELTFEILRDLVDDIVTVSEDEIAAAMRLLLERT----KIVVEP 280

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 491001101 340 SGAVGLGilsAVHFHPQRealmnklgLDSRSVVLVIStEGDTDVEHYREVVWEG 393
Cdd:COG1171  281 AGAAALA---ALLAGKER--------LKGKRVVVVLS-GGNIDPDRLAEILERG 322
PALP pfam00291
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ...
 41-378 1.51e-41

Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate dependent enzymes. This family includes: serine dehydratase EC:4.2.1.13 P20132, threonine dehydratase EC:4.2.1.16, tryptophan synthase beta chain EC:4.2.1.20, threonine synthase EC:4.2.99.2, cysteine synthase EC:4.2.99.8 P11096, cystathionine beta-synthase EC:4.2.1.22, 1-aminocyclopropane-1-carboxylate deaminase EC:4.1.99.4.


Pssm-ID: 459749 [Multi-domain]  Cd Length: 295  Bit Score: 148.23  E-value: 1.51e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491001101   41 GYKPTPLYALKSLAALFGVStILVKDES-QRFGlnAFKMLGGAYAIAQLLcekyhldinafsfatfksSIKEKMTFATTT 119
Cdd:pfam00291   4 GIGPTPLVRLPRLSKELGVD-VYLKLESlNPTG--SFKDRGALNLLLRLK------------------EGEGGKTVVEAS 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491001101  120 DGNHGRGVAWAAQQLGQNAVIYMPKGSAQERVDAILRLGARCIVTEMNYDDTVRFTMQTARQngwevvqdtaWEGYTKIP 199
Cdd:pfam00291  63 SGNHGRALAAAAARLGLKVTIVVPEDAPPGKLLLMRALGAEVVLVGGDYDEAVAAARELAAE----------GPGAYYIN 132

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491001101  200 ----TWIMQGYATLADEAVEQMAamgiARPTHVFLQAGVGAMAGGVLGYLVDVFGARDLhsVIVEPELADCLYRSGVKGQ 275
Cdd:pfam00291 133 qydnPLNIEGYGTIGLEILEQLG----GDPDAVVVPVGGGGLIAGIARGLKELGPDVRV--IGVEPEGAPALARSLAAGR 206

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491001101  276 IVNVgGSMATIMAGLACG-EPNPLGWDILRNCATQFISCQDAVAALGMRVLGNPLGtdprVISGESGAVGLGILSAVhfh 354
Cdd:pfam00291 207 PVPV-PVADTIADGLGVGdEPGALALDLLDEYVGEVVTVSDEEALEAMRLLARREG----IVVEPSSAAALAALKLA--- 278

                         330       340
                  ....*....|....*....|....
gi 491001101  355 pqrealmNKLGLDSRSVVLVISTE 378
Cdd:pfam00291 279 -------LAGELKGGDRVVVVLTG 295
Trp-synth-beta_II cd00640
Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP) ...
 45-262 2.65e-31

Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP)-dependent enzymes catalyzes beta-replacement and beta-elimination reactions. This CD corresponds to aminocyclopropane-1-carboxylate deaminase (ACCD), tryptophan synthase beta chain (Trp-synth_B), cystathionine beta-synthase (CBS), O-acetylserine sulfhydrylase (CS), serine dehydratase (Ser-dehyd), threonine dehydratase (Thr-dehyd), diaminopropionate ammonia lyase (DAL), and threonine synthase (Thr-synth). ACCD catalyzes the conversion of 1-aminocyclopropane-1-carboxylate to alpha-ketobutyrate and ammonia. Tryptophan synthase folds into a tetramer, where the beta chain is the catalytic PLP-binding subunit and catalyzes the formation of L-tryptophan from indole and L-serine. CBS is a tetrameric hemeprotein that catalyzes condensation of serine and homocysteine to cystathionine. CS is a homodimer that catalyzes the formation of L-cysteine from O-acetyl-L-serine. Ser-dehyd catalyzes the conversion of L- or D-serine to pyruvate and ammonia. Thr-dehyd is active as a homodimer and catalyzes the conversion of L-threonine to 2-oxobutanoate and ammonia. DAL is also a homodimer and catalyzes the alpha, beta-elimination reaction of both L- and D-alpha, beta-diaminopropionate to form pyruvate and ammonia. Thr-synth catalyzes the formation of threonine and inorganic phosphate from O-phosphohomoserine.


Pssm-ID: 107202 [Multi-domain]  Cd Length: 244  Bit Score: 119.16  E-value: 2.65e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491001101  45 TPLYALKSLAALFGVsTILVKDESQRFGLnAFKMLGGAYAIAQLLcekyhldinafsfatfKSSIKEKMTFATTTDGNHG 124
Cdd:cd00640    1 TPLVRLKRLSKLGGA-NIYLKLEFLNPTG-SFKDRGALNLILLAE----------------EEGKLPKGVIIESTGGNTG 62

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491001101 125 RGVAWAAQQLGQNAVIYMPKGSAQERVDAILRLGARCIVTEMNYDDTVRFTMQ-TARQNGWEVVQDTawegytkIPTWIM 203
Cdd:cd00640   63 IALAAAAARLGLKCTIVMPEGASPEKVAQMRALGAEVVLVPGDFDDAIALAKElAEEDPGAYYVNQF-------DNPANI 135

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 491001101 204 QGYATLADEAVEQMAAMgiaRPTHVFLQAGVGAMAGGVLGYLVDvfGARDLHSVIVEPE 262
Cdd:cd00640  136 AGQGTIGLEILEQLGGQ---KPDAVVVPVGGGGNIAGIARALKE--LLPNVKVIGVEPE 189
 
Name Accession Description Interval E-value
2_3_DAP_am_ly TIGR03528
diaminopropionate ammonia-lyase; Members of this protein family are the homodimeric, pyridoxal ...
 5-393 0e+00

diaminopropionate ammonia-lyase; Members of this protein family are the homodimeric, pyridoxal phosphate enzyme diaminopropionate ammonia-lyase, which adds water to remove two amino groups, leaving pyruvate.


Pssm-ID: 274631  Cd Length: 396  Bit Score: 702.63  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491001101    5 SLKMDIAENRF-FTGETSPLFSRQQAQQARHFHQKIVGYKPTPLYALKSLAALFGVSTILVKDESQRFGLNAFKMLGGAY 83
Cdd:TIGR03528   1 SIKIIINDNKKaTNGTDLSLLSKEEAEKVRAFHQSFPGYQPTPLAELDNLAKHLGVGSILVKDESYRFGLNAFKVLGGSY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491001101   84 AIAQLLCEKYHLDINAFSFATFKSS-IKEKM---TFATTTDGNHGRGVAWAAQQLGQNAVIYMPKGSAQERVDAILRLGA 159
Cdd:TIGR03528  81 AIGKYLAEKLGKDISELSFEKLKSNeIREKLgdiTFVTATDGNHGRGVAWAANQLGQKSVVYMPKGSAQERLENIRAEGA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491001101  160 RCIVTEMNYDDTVRFTMQTARQNGWEVVQDTAWEGYTKIPTWIMQGYATLADEAVEQMAAMGIARPTHVFLQAGVGAMAG 239
Cdd:TIGR03528 161 ECTITDLNYDDAVRLAWKMAQENGWVMVQDTAWEGYEKIPTWIMQGYGTLALEALEQLKEQGVEKPTHVFLQAGVGSFAG 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491001101  240 GVLGYLVDVFGARDLHSVIVEPELADCLYRSGVK--GQIVNVGGSMATIMAGLACGEPNPLGWDILRNCATQFISCQDAV 317
Cdd:TIGR03528 241 AVQGYFASVYGEERPITVIVEPDKADCIYRSAIAddGKPHFVTGDMATIMAGLACGEPNTIGWEILRDYASQFISCPDWV 320

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491001101  318 AALGMRVLGNPLGTDPRVISGESGAVGLGILSAVHFHPQREALMNKLGLDSRSVVLVISTEGDTDVEHYREVVWEG 393
Cdd:TIGR03528 321 AAKGMRILGNPLKGDPRVISGESGAVGTGLLAAVMTHPDYKELREKLQLDKNSRVLLISTEGDTDPDHYRKIVWNG 396
PRK08206 PRK08206
diaminopropionate ammonia-lyase; Provisional
 1-396 0e+00

diaminopropionate ammonia-lyase; Provisional


Pssm-ID: 236186  Cd Length: 399  Bit Score: 681.99  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491001101   1 MSAFSLKMDIAENRFFTGETSPLFSRQQAQQARHFHQKIVGYKPTPLYALKSLAALFGVSTILVKDESQRFGLNAFKMLG 80
Cdd:PRK08206   1 MSMFLLKNNIADNKPYDGADLPLLSQEEAKKARAFHQSFPGYAPTPLVALPDLAAELGVGSILVKDESYRFGLNAFKALG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491001101  81 GAYAIAQLLCEKYHLDINAFSFATFKS----SIKEKMTFATTTDGNHGRGVAWAAQQLGQNAVIYMPKGSAQERVDAILR 156
Cdd:PRK08206  81 GAYAVARLLAEKLGLDISELSFEELTSgevrEKLGDITFATATDGNHGRGVAWAAQQLGQKAVIYMPKGSSEERVDAIRA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491001101 157 LGARCIVTEMNYDDTVRFTMQTARQNGWEVVQDTAWEGYTKIPTWIMQGYATLADEAVEQMAAMGiARPTHVFLQAGVGA 236
Cdd:PRK08206 161 LGAECIITDGNYDDSVRLAAQEAQENGWVVVQDTAWEGYEEIPTWIMQGYGTMADEAVEQLKEMG-VPPTHVFLQAGVGS 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491001101 237 MAGGVLGYLVDVFGARDLHSVIVEPELADCLYRSGVKGQIVNVGGSMATIMAGLACGEPNPLGWDILRNCATQFISCQDA 316
Cdd:PRK08206 240 LAGAVLGYFAEVYGEQRPHFVVVEPDQADCLYQSAVDGKPVAVTGDMDTIMAGLACGEPNPLAWEILRNCADAFISCPDE 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491001101 317 VAALGMRVLGNPLGTDPRVISGESGAVGLGILSAVHFHPQREALMNKLGLDSRSVVLVISTEGDTDVEHYREVVWEGKYP 396
Cdd:PRK08206 320 VAALGMRILANPLGGDPPIVSGESGAVGLGALAALMTDPDYQELREKLGLDEDSRVLLISTEGDTDPDRYREIVWEGKYA 399
diampropi_NH3ly TIGR01747
diaminopropionate ammonia-lyase family; This small subfamily includes diaminopropionate ...
 23-392 0e+00

diaminopropionate ammonia-lyase family; This small subfamily includes diaminopropionate ammonia-lyase from Salmonella typhimurium and a small number of close homologs, about 50 % identical in sequence. The enzyme is a pyridoxal phosphate-binding homodimer homologous to threonine dehydratase (threonine deaminase). [Energy metabolism, Other]


Pssm-ID: 130808  Cd Length: 376  Bit Score: 618.83  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491001101   23 LFSRQQAQQARHFHQKIVGYKPTPLYALKSLAALFGVSTILVKDESQRFGLNAFKMLGGAYAIAQLLCEKYHLDINAFSF 102
Cdd:TIGR01747   1 LFSQSQAKLALAFHKKIPGYRPTPLCALDHLANLLGLKKILVKDESKRFGLNAFKMLGGSYAIAQYLAEKLHLDIETLSF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491001101  103 ATFKS-SIKEKM---TFATTTDGNHGRGVAWAAQQLGQNAVIYMPKGSAQERVDAILRLGARCIVTEMNYDDTVRFTMQT 178
Cdd:TIGR01747  81 EHLKNdAIGEKMgqaTFATATDGNHGRGVAWAAQQLGQKAVVYMPKGSAQERVENILNLGAECTITDMNYDDTVRLAMQM 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491001101  179 ARQNGWEVVQDTAWEGYTKIPTWIMQGYATLADEAVEQMAAMGIARPTHVFLQAGVGAMAGGVLGYLVDVFGARDLHSVI 258
Cdd:TIGR01747 161 AQQHGWVVVQDTAWEGYEKIPTWIMQGYATLADEAVEQLREMGSVTPTHVLLQAGVGSMAGGVLGYFVDVYSENNPHSIV 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491001101  259 VEPELADCLYRSGVK--GQIVNVGGSMATIMAGLACGEPNPLGWDILRNCATQFISCQDAVAALGMRVLGNPLGTDPRVI 336
Cdd:TIGR01747 241 VEPDKADCLYQSAVKkdGDIVNVGGDMATIMAGLACGEPNPISWEILRNCTSQFISAQDSVAAKGMRVLGAPYGGDPRII 320

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 491001101  337 SGESGAVGLGILSAVHFHPQREALMNKLGLDSRSVVLVISTEGDTDVEHYREVVWE 392
Cdd:TIGR01747 321 SGESGAVGLGLLAAVMYHPQYQSLMEKLQLDKDAVVLVISTEGDTDPDHYREIVWE 376
IlvA COG1171
Threonine deaminase [Amino acid transport and metabolism]; Threonine deaminase is part of the ...
 20-393 3.14e-93

Threonine deaminase [Amino acid transport and metabolism]; Threonine deaminase is part of the Pathway/BioSystem: Isoleucine, leucine, valine biosynthesis


Pssm-ID: 440784 [Multi-domain]  Cd Length: 327  Bit Score: 282.70  E-value: 3.14e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491001101  20 TSPLFSRQQAQQARHFHQKIVgyKPTPLYALKSLAALFGvSTILVKDESQRFgLNAFKMLGGAYAIAQLlcekyhldina 99
Cdd:COG1171    2 TALMPTLADIEAAAARIAGVV--RRTPLLRSPTLSERLG-AEVYLKLENLQP-TGSFKLRGAYNALASL----------- 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491001101 100 fsfatfkSSIKEKMTFATTTDGNHGRGVAWAAQQLGQNAVIYMPKGSAQERVDAILRLGARCIVTEMNYDDTVRFTMQTA 179
Cdd:COG1171   67 -------SEEERARGVVAASAGNHAQGVAYAARLLGIPATIVMPETAPAVKVAATRAYGAEVVLHGDTYDDAEAAAAELA 139

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491001101 180 RQNGWEVVQDTAwegytkiPTWIMQGYATLADEAVEQMAAmgiarPTHVFLQAGVGAMAGGVLGYLVDVfgARDLHSVIV 259
Cdd:COG1171  140 EEEGATFVHPFD-------DPDVIAGQGTIALEILEQLPD-----LDAVFVPVGGGGLIAGVAAALKAL--SPDIRVIGV 205

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491001101 260 EPELADCLYRSGVKGQIVNVGGsMATIMAGLACGEPNPLGWDILRNCATQFISCQDAVAALGMRVLGNPLgtdpRVISGE 339
Cdd:COG1171  206 EPEGAAAMYRSLAAGEPVTLPG-VDTIADGLAVGRPGELTFEILRDLVDDIVTVSEDEIAAAMRLLLERT----KIVVEP 280

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 491001101 340 SGAVGLGilsAVHFHPQRealmnklgLDSRSVVLVIStEGDTDVEHYREVVWEG 393
Cdd:COG1171  281 AGAAALA---ALLAGKER--------LKGKRVVVVLS-GGNIDPDRLAEILERG 322
PALP pfam00291
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ...
 41-378 1.51e-41

Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate dependent enzymes. This family includes: serine dehydratase EC:4.2.1.13 P20132, threonine dehydratase EC:4.2.1.16, tryptophan synthase beta chain EC:4.2.1.20, threonine synthase EC:4.2.99.2, cysteine synthase EC:4.2.99.8 P11096, cystathionine beta-synthase EC:4.2.1.22, 1-aminocyclopropane-1-carboxylate deaminase EC:4.1.99.4.


Pssm-ID: 459749 [Multi-domain]  Cd Length: 295  Bit Score: 148.23  E-value: 1.51e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491001101   41 GYKPTPLYALKSLAALFGVStILVKDES-QRFGlnAFKMLGGAYAIAQLLcekyhldinafsfatfksSIKEKMTFATTT 119
Cdd:pfam00291   4 GIGPTPLVRLPRLSKELGVD-VYLKLESlNPTG--SFKDRGALNLLLRLK------------------EGEGGKTVVEAS 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491001101  120 DGNHGRGVAWAAQQLGQNAVIYMPKGSAQERVDAILRLGARCIVTEMNYDDTVRFTMQTARQngwevvqdtaWEGYTKIP 199
Cdd:pfam00291  63 SGNHGRALAAAAARLGLKVTIVVPEDAPPGKLLLMRALGAEVVLVGGDYDEAVAAARELAAE----------GPGAYYIN 132

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491001101  200 ----TWIMQGYATLADEAVEQMAamgiARPTHVFLQAGVGAMAGGVLGYLVDVFGARDLhsVIVEPELADCLYRSGVKGQ 275
Cdd:pfam00291 133 qydnPLNIEGYGTIGLEILEQLG----GDPDAVVVPVGGGGLIAGIARGLKELGPDVRV--IGVEPEGAPALARSLAAGR 206

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491001101  276 IVNVgGSMATIMAGLACG-EPNPLGWDILRNCATQFISCQDAVAALGMRVLGNPLGtdprVISGESGAVGLGILSAVhfh 354
Cdd:pfam00291 207 PVPV-PVADTIADGLGVGdEPGALALDLLDEYVGEVVTVSDEEALEAMRLLARREG----IVVEPSSAAALAALKLA--- 278

                         330       340
                  ....*....|....*....|....
gi 491001101  355 pqrealmNKLGLDSRSVVLVISTE 378
Cdd:pfam00291 279 -------LAGELKGGDRVVVVLTG 295
Trp-synth-beta_II cd00640
Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP) ...
 45-262 2.65e-31

Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP)-dependent enzymes catalyzes beta-replacement and beta-elimination reactions. This CD corresponds to aminocyclopropane-1-carboxylate deaminase (ACCD), tryptophan synthase beta chain (Trp-synth_B), cystathionine beta-synthase (CBS), O-acetylserine sulfhydrylase (CS), serine dehydratase (Ser-dehyd), threonine dehydratase (Thr-dehyd), diaminopropionate ammonia lyase (DAL), and threonine synthase (Thr-synth). ACCD catalyzes the conversion of 1-aminocyclopropane-1-carboxylate to alpha-ketobutyrate and ammonia. Tryptophan synthase folds into a tetramer, where the beta chain is the catalytic PLP-binding subunit and catalyzes the formation of L-tryptophan from indole and L-serine. CBS is a tetrameric hemeprotein that catalyzes condensation of serine and homocysteine to cystathionine. CS is a homodimer that catalyzes the formation of L-cysteine from O-acetyl-L-serine. Ser-dehyd catalyzes the conversion of L- or D-serine to pyruvate and ammonia. Thr-dehyd is active as a homodimer and catalyzes the conversion of L-threonine to 2-oxobutanoate and ammonia. DAL is also a homodimer and catalyzes the alpha, beta-elimination reaction of both L- and D-alpha, beta-diaminopropionate to form pyruvate and ammonia. Thr-synth catalyzes the formation of threonine and inorganic phosphate from O-phosphohomoserine.


Pssm-ID: 107202 [Multi-domain]  Cd Length: 244  Bit Score: 119.16  E-value: 2.65e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491001101  45 TPLYALKSLAALFGVsTILVKDESQRFGLnAFKMLGGAYAIAQLLcekyhldinafsfatfKSSIKEKMTFATTTDGNHG 124
Cdd:cd00640    1 TPLVRLKRLSKLGGA-NIYLKLEFLNPTG-SFKDRGALNLILLAE----------------EEGKLPKGVIIESTGGNTG 62

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491001101 125 RGVAWAAQQLGQNAVIYMPKGSAQERVDAILRLGARCIVTEMNYDDTVRFTMQ-TARQNGWEVVQDTawegytkIPTWIM 203
Cdd:cd00640   63 IALAAAAARLGLKCTIVMPEGASPEKVAQMRALGAEVVLVPGDFDDAIALAKElAEEDPGAYYVNQF-------DNPANI 135

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 491001101 204 QGYATLADEAVEQMAAMgiaRPTHVFLQAGVGAMAGGVLGYLVDvfGARDLHSVIVEPE 262
Cdd:cd00640  136 AGQGTIGLEILEQLGGQ---KPDAVVVPVGGGGNIAGIARALKE--LLPNVKVIGVEPE 189
Thr-dehyd cd01562
Threonine dehydratase: The first step in amino acid degradation is the removal of nitrogen. ...
 36-376 1.76e-28

Threonine dehydratase: The first step in amino acid degradation is the removal of nitrogen. Although the nitrogen atoms of most amino acids are transferred to alpha-ketoglutarate before removal, the alpha-amino group of threonine can be directly converted into NH4+. The direct deamination is catalyzed by threonine dehydratase, in which pyridoxal phosphate (PLP) is the prosthetic group. Threonine dehydratase is widely distributed in all three major phylogenetic divisions.


Pssm-ID: 107205 [Multi-domain]  Cd Length: 304  Bit Score: 113.35  E-value: 1.76e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491001101  36 HQKIVGY-KPTPLYALKSLAALFGVsTILVKDES-QRFGlnAFKMLGGAYAIAQLLCEKYHLDINAFSfatfkssikekm 113
Cdd:cd01562    8 AARIKPVvRRTPLLTSPTLSELLGA-EVYLKCENlQKTG--SFKIRGAYNKLLSLSEEERAKGVVAAS------------ 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491001101 114 tfatttDGNHGRGVAWAAQQLGQNAVIYMPKGSAQERVDAILRLGARCIVTEMNYDDTVRFTMQTARQngwevvqdtawE 193
Cdd:cd01562   73 ------AGNHAQGVAYAAKLLGIPATIVMPETAPAAKVDATRAYGAEVVLYGEDFDEAEAKARELAEE-----------E 135

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491001101 194 GYTKIPT----WIMQGYATLADEAVEQMAAmgiarPTHVFLQAGVGAMAGGVLGYL------VDVFGardlhsviVEPEL 263
Cdd:cd01562  136 GLTFIHPfddpDVIAGQGTIGLEILEQVPD-----LDAVFVPVGGGGLIAGIATAVkalspnTKVIG--------VEPEG 202

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491001101 264 ADCLYRSGVKGQIVNVgGSMATIMAGLACGEPNPLGWDILRNCATQFISCQDAVAALGMRVlgnpLGTDPRVISGESGAV 343
Cdd:cd01562  203 APAMAQSLAAGKPVTL-PEVDTIADGLAVKRPGELTFEIIRKLVDDVVTVSEDEIAAAMLL----LFEREKLVAEPAGAL 277

                        330       340       350
                 ....*....|....*....|....*....|....
gi 491001101 344 GLGilsavhfhpqreALMN-KLGLDSRSVVLVIS 376
Cdd:cd01562  278 ALA------------ALLSgKLDLKGKKVVVVLS 299
PRK09224 PRK09224
threonine ammonia-lyase IlvA;
45-277 1.46e-15

threonine ammonia-lyase IlvA;


Pssm-ID: 236417 [Multi-domain]  Cd Length: 504  Bit Score: 78.26  E-value: 1.46e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491001101  45 TPLYALKSLAALFGvSTILVKDESQR--FglnAFKmLGGAYA-IAQLLCEKYHLDINAFSfatfkssikekmtfAtttdG 121
Cdd:PRK09224  21 TPLEKAPKLSARLG-NQVLLKREDLQpvF---SFK-LRGAYNkMAQLTEEQLARGVITAS--------------A----G 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491001101 122 NHGRGVAWAAQQLGQNAVIYMPKGSAQERVDAILRLGARCIVTEMNYDDTVRFTMQTARQngwevvqdtawEGYTKIPTW 201
Cdd:PRK09224  78 NHAQGVALSAARLGIKAVIVMPVTTPDIKVDAVRAFGGEVVLHGDSFDEAYAHAIELAEE-----------EGLTFIHPF 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491001101 202 ----IMQGYATLADEAVEQMAamgiARPTHVFLQAGVGAMAGGVLGYL------VDVFGardlhsviVEPELADCLYRSG 271
Cdd:PRK09224 147 ddpdVIAGQGTIAMEILQQHP----HPLDAVFVPVGGGGLIAGVAAYIkqlrpeIKVIG--------VEPEDSACLKAAL 214


                 ....*.
gi 491001101 272 VKGQIV 277
Cdd:PRK09224 215 EAGERV 220
PRK08639 PRK08639
threonine dehydratase; Validated
 49-277 3.00e-14

threonine dehydratase; Validated


Pssm-ID: 236318 [Multi-domain]  Cd Length: 420  Bit Score: 73.69  E-value: 3.00e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491001101  49 ALKSLAALFgVSTILVKDE--SQRFGLN------------AFKMLGGAYAIAQLlcekyhldinafsfatfkSSIKEKMT 114
Cdd:PRK08639  15 AAKRLKDVV-PETPLQRNDylSEKYGANvylkredlqpvrSYKLRGAYNAISQL------------------SDEELAAG 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491001101 115 FATTTDGNHGRGVAWAAQQLGQNAVIYMPKGSAQERVDAILRLGA---RCIVTEMNYDDTVRftmqtarqngwEVVQDTA 191
Cdd:PRK08639  76 VVCASAGNHAQGVAYACRHLGIPGVIFMPVTTPQQKIDQVRFFGGefvEIVLVGDTFDDSAA-----------AAQEYAE 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491001101 192 WEGYTKIPTW----IMQGYATLADEAVEQMAAMGiaRPTHVFLQAGVGAMAGGVLGYLVDVfgARDLHSVIVEPELADCL 267
Cdd:PRK08639 145 ETGATFIPPFddpdVIAGQGTVAVEILEQLEKEG--SPDYVFVPVGGGGLISGVTTYLKER--SPKTKIIGVEPAGAASM 220

                        250
                 ....*....|
gi 491001101 268 YRSGVKGQIV 277
Cdd:PRK08639 221 KAALEAGKPV 230
THD1 TIGR02079
threonine dehydratase; This model represents threonine dehydratase, the first step in the ...
 27-277 2.91e-13

threonine dehydratase; This model represents threonine dehydratase, the first step in the pathway converting threonine into isoleucine. At least two other clades of biosynthetic threonine dehydratases have been characterized by models (TIGR01124 and TIGR01127). Those sequences described by this model are exclusively found in species containg the rest of the isoleucine pathway and which are generally lacking in members of the those other two clades of threonine dehydratases. Members of this clade are also often gene clustered with other elements of the isoleucine pathway. [Amino acid biosynthesis, Pyruvate family]


Pssm-ID: 273957 [Multi-domain]  Cd Length: 409  Bit Score: 70.55  E-value: 2.91e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491001101   27 QQAQQARHFHQKIVgyKPTPLYALKSLAALFGVSTILVKDESQRfgLNAFKMLGGAYAIAQLlcekyhldinafsfatfk 106
Cdd:TIGR02079   1 QDIEAARKRLKEVV--PHTPLQLNERLSEKYGANIYLKREDLQP--VRSYKIRGAYNFLKQL------------------ 58

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491001101  107 SSIKEKMTFATTTDGNHGRGVAWAAQQLGQNAVIYMPKGSAQERVDAILRLGARCIvtemnyddTVRFTMQTARQNGWEV 186
Cdd:TIGR02079  59 SDAQLAKGVVCASAGNHAQGFAYACRHLGVHGTVFMPATTPKQKIDRVKIFGGEFI--------EIILVGDTFDQCAAAA 130

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491001101  187 VQDTAWEGYTKIPTW----IMQGYATLADEAVEQMAamgiARPTHVFLQAGVGAMAGGVLGYLVDVfgARDLHSVIVEPE 262
Cdd:TIGR02079 131 REHVEDHGGTFIPPFddprIIEGQGTVAAEILDQLP----EKPDYVVVPVGGGGLISGLTTYLAGT--SPKTKIIGVEPE 204

                         250
                  ....*....|....*
gi 491001101  263 LADCLYRSGVKGQIV 277
Cdd:TIGR02079 205 GAPSMKASLEAGEVV 219
eutB PRK07476
threonine dehydratase; Provisional
 45-241 3.76e-13

threonine dehydratase; Provisional


Pssm-ID: 236025 [Multi-domain]  Cd Length: 322  Bit Score: 69.61  E-value: 3.76e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491001101  45 TPLYALKSLAALFGVSTILVKDESQRFGlnAFKMLGGAYAIAQLLCEKYHLDINAFSfatfkssikekmtfatttDGNHG 124
Cdd:PRK07476  20 TPLVASASLSARAGVPVWLKLETLQPTG--SFKLRGATNALLSLSAQERARGVVTAS------------------TGNHG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491001101 125 RGVAWAAQQLGQNAVIYMPKGSAQERVDAILRLGARCIVTEMNYDDtvrftmqtARQngwEVVQDTAWEGYTKIPTW--- 201
Cdd:PRK07476  80 RALAYAARALGIRATICMSRLVPANKVDAIRALGAEVRIVGRSQDD--------AQA---EVERLVREEGLTMVPPFddp 148

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 491001101 202 -IMQGYATLADEAVEQMAAMGIarpthVFLQAGVGAMAGGV 241
Cdd:PRK07476 149 rIIAGQGTIGLEILEALPDVAT-----VLVPLSGGGLASGV 184
PRK06815 PRK06815
threonine/serine dehydratase;
36-341 8.98e-13

threonine/serine dehydratase;


Pssm-ID: 180709 [Multi-domain]  Cd Length: 317  Bit Score: 68.57  E-value: 8.98e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491001101  36 HQKIVGY-KPTPLYALKSLAALFGVSTILVKDESQRFGlnAFKMLGGAYAIAQLlcekyhldinafsfatfkSSIKEKMT 114
Cdd:PRK06815  11 HQRLRPQvRVTPLEHSPLLSQHTGCEVYLKCEHLQHTG--SFKFRGASNKLRLL------------------NEAQRQQG 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491001101 115 FATTTDGNHGRGVAWAAQQLGQNAVIYMPKGSAQERVDAILRLGARCIVTEmnyDDTVRFTMQTARQngwevvqdTAWEG 194
Cdd:PRK06815  71 VITASSGNHGQGVALAAKLAGIPVTVYAPEQASAIKLDAIRALGAEVRLYG---GDALNAELAARRA--------AEQQG 139

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491001101 195 YTKIPTW----IMQGYATLADEAVEQmaamgIARPTHVFLQAGVGAMAGGVLGYLVDVfgARDLHSVIVEPELADCLYRS 270
Cdd:PRK06815 140 KVYISPYndpqVIAGQGTIGMELVEQ-----QPDLDAVFVAVGGGGLISGIATYLKTL--SPKTEIIGCWPANSPSLYTS 212

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491001101 271 GVKGQIVNVgGSMATIMAGLACG-EPNPLGWDILRNCATQFISCQDAVAALGMRVLgnpLGTDPRVISGESG 341
Cdd:PRK06815 213 LEAGEIVEV-AEQPTLSDGTAGGvEPGAITFPLCQQLIDQKVLVSEEEIKEAMRLI---AETDRWLIEGAAG 280
PRK06110 PRK06110
threonine dehydratase;
22-325 1.63e-12

threonine dehydratase;


Pssm-ID: 235699  Cd Length: 322  Bit Score: 67.71  E-value: 1.63e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491001101  22 PLFSRQQAQQARhfhqKIVG--YKPTPLYALKSLAALFGvSTILVKDESQRfGLNAFKMLGGAYAIAQLLCEKyhldina 99
Cdd:PRK06110   1 MMFTLAELEAAA----AVVYaaMPPTPQYRWPLLAERLG-CEVWVKHENHT-PTGAFKVRGGLVYFDRLARRG------- 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491001101 100 fsfATFKSSIkekmtfaTTTDGNHGRGVAWAAQQLGQNAVIYMPKGSAQERVDAILRLGARCIVTEMNYDDTVRFTMQTA 179
Cdd:PRK06110  68 ---PRVRGVI-------SATRGNHGQSVAFAARRHGLAATIVVPHGNSVEKNAAMRALGAELIEHGEDFQAAREEAARLA 137

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491001101 180 RQNGWEVVqdtawegytkiPT---WIMQGYATLADEAVEQMAAMGIarpthVFLQAGVGAmagGVLGylvdVFGARDL-- 254
Cdd:PRK06110 138 AERGLHMV-----------PSfhpDLVRGVATYALELFRAVPDLDV-----VYVPIGMGS---GICG----AIAARDAlg 194

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491001101 255 ---HSVIVEPELADCLYRSGVKGQIVNVggSMATIMA-GLACGEPNPLGWDILRNCATQFISCQDAVAALGMRVL 325
Cdd:PRK06110 195 lktRIVGVVSAHAPAYALSFEAGRVVTT--PVATTLAdGMACRTPDPEALEVIRAGADRIVRVTDDEVAAAMRAY 267
PLN02550 PLN02550
threonine dehydratase
 45-281 2.91e-11

threonine dehydratase


Pssm-ID: 178165 [Multi-domain]  Cd Length: 591  Bit Score: 64.94  E-value: 2.91e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491001101  45 TPLYALKSLAALFGVSTILVKDESQRfgLNAFKMLGGAYAIAQLLCEKYHldinafsfatfKSSIkekmtfaTTTDGNHG 124
Cdd:PLN02550 110 SPLQLAKKLSERLGVKVLLKREDLQP--VFSFKLRGAYNMMAKLPKEQLD-----------KGVI-------CSSAGNHA 169

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491001101 125 RGVAWAAQQLGQNAVIYMPKGSAQERVDAILRLGARCIVTEMNYDDTVRFTMQTARQngwevvqdtawEGYTKIPTW--- 201
Cdd:PLN02550 170 QGVALSAQRLGCDAVIAMPVTTPEIKWQSVERLGATVVLVGDSYDEAQAYAKQRALE-----------EGRTFIPPFdhp 238

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491001101 202 -IMQGYATLADEAVEQMAAmgiarPTH-VFLQAGVGAMAGGVLGYLVDVfgARDLHSVIVEPELADCLYRSGVKGQIV-- 277
Cdd:PLN02550 239 dVIAGQGTVGMEIVRQHQG-----PLHaIFVPVGGGGLIAGIAAYVKRV--RPEVKIIGVEPSDANAMALSLHHGERVml 311


                 ....*
gi 491001101 278 -NVGG 281
Cdd:PLN02550 312 dQVGG 316
Thr-synth_1 cd01563
Threonine synthase is a pyridoxal phosphate (PLP) dependent enzyme that catalyses the last ...
 45-316 3.20e-11

Threonine synthase is a pyridoxal phosphate (PLP) dependent enzyme that catalyses the last reaction in the synthesis of threonine from aspartate. It proceeds by converting O-phospho-L-homoserine (OPH) into threonine and inorganic phosphate. In plants, OPH is an intermediate between the methionine and threonine/isoleucine pathways. Thus threonine synthase competes for OPH with cystathionine-gamma-synthase, the first enzyme in the methionine pathway. These enzymes are in general dimers. Members of this CD, Thr-synth_1, are widely distributed in bacteria, archaea and higher plants.


Pssm-ID: 107206 [Multi-domain]  Cd Length: 324  Bit Score: 63.77  E-value: 3.20e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491001101  45 TPLYALKSLAALFGVSTILVKDEsqrfGLN---AFKMLGGAYAIAQLLcekyHLDINafsfatfkssikekmTFATTTDG 121
Cdd:cd01563   23 TPLVRAPRLGERLGGKNLYVKDE----GLNptgSFKDRGMTVAVSKAK----ELGVK---------------AVACASTG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491001101 122 NHGRGVAWAAQQLGQNAVIYMPKGSAQERVDAILRLGARCIVTEMNYDDTVRFTMQTARQNGWEVVqdtawegyTKIPTW 201
Cdd:cd01563   80 NTSASLAAYAARAGIKCVVFLPAGKALGKLAQALAYGATVLAVEGNFDDALRLVRELAEENWIYLS--------NSLNPY 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491001101 202 IMQGYATLADEAVEQmaaMGIARPTHVFLQAGVGamaGGVLGYLVdvfGARDLHS----------VIVEPELADCLYRSG 271
Cdd:cd01563  152 RLEGQKTIAFEIAEQ---LGWEVPDYVVVPVGNG---GNITAIWK---GFKELKElglidrlprmVGVQAEGAAPIVRAF 222

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 491001101 272 VKGQ-IVNVGGSMATIMAGLACGepNPLGWD----ILRNCATQFISCQDA 316
Cdd:cd01563  223 KEGKdDIEPVENPETIATAIRIG--NPASGPkalrAVRESGGTAVAVSDE 270
PRK06381 PRK06381
threonine synthase; Validated
 101-241 6.23e-11

threonine synthase; Validated


Pssm-ID: 235789  Cd Length: 319  Bit Score: 63.19  E-value: 6.23e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491001101 101 SFATFKSSIKEKM-TFATTTDGNHGRGVAWAAQQLGQNAVIYMPKGSAQERVDAILRLGARCIVTEMNYDDTVRFTMQTA 179
Cdd:PRK06381  51 AEAHVRRAMRLGYsGITVGTCGNYGASIAYFARLYGLKAVIFIPRSYSNSRVKEMEKYGAEIIYVDGKYEEAVERSRKFA 130

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491001101 180 RQNGWevvqdtawegYTKIP----TWI-MQGYATLADEAVEQMAAMgiarPTHVFLQAGVGAMAGGV 241
Cdd:PRK06381 131 KENGI----------YDANPgsvnSVVdIEAYSAIAYEIYEALGDV----PDAVAVPVGNGTTLAGI 183
PLN02970 PLN02970
serine racemase
 36-392 7.70e-11

serine racemase


Pssm-ID: 215524 [Multi-domain]  Cd Length: 328  Bit Score: 62.77  E-value: 7.70e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491001101  36 HQKIVGY-KPTPLYALKSLAALFGVSTILVKDESQRFGlnAFKMLGGAYAIAQLLCEKyhldiNAFSFATFKSsikekmt 114
Cdd:PLN02970  18 RKRIAPFiHRTPVLTSSSLDALAGRSLFFKCECFQKGG--AFKFRGACNAIFSLSDDQ-----AEKGVVTHSS------- 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491001101 115 fatttdGNHGRGVAWAAQQLGQNAVIYMPKGSAQERVDAILRLGARCIVTEMnyddtvrfTMQTARQNGWEVVQDTaweG 194
Cdd:PLN02970  84 ------GNHAAALALAAKLRGIPAYIVVPKNAPACKVDAVIRYGGIITWCEP--------TVESREAVAARVQQET---G 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491001101 195 YTKIPTW----IMQGYATLADEAVEQMAAMGIarpthVFLQAGVGAMAGGVlgylvdVFGARDLHSVI----VEPELADC 266
Cdd:PLN02970 147 AVLIHPYndgrVISGQGTIALEFLEQVPELDV-----IIVPISGGGLISGI------ALAAKAIKPSIkiiaAEPKGADD 215

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491001101 267 LYRSGVKGQIVnvggSMA---TIMAGLAcGEPNPLGWDILRNCATQFISCQDAVAALGMRVLGNPLgtdpRVISGESGAV 343
Cdd:PLN02970 216 AAQSKAAGEII----TLPvtnTIADGLR-ASLGDLTWPVVRDLVDDVITVDDKEIIEAMKLCYERL----KVVVEPSGAI 286

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|
gi 491001101 344 GL-GILSavhfhpqREALMNKLGLDSRSVVLVISTeGDTDVehyrEVVWE 392
Cdd:PLN02970 287 GLaAALS-------DSFRSNPAWKGCKNVGIVLSG-GNVDL----GVLWE 324
PRK06608 PRK06608
serine/threonine dehydratase;
36-291 1.40e-09

serine/threonine dehydratase;


Pssm-ID: 235842 [Multi-domain]  Cd Length: 338  Bit Score: 59.01  E-value: 1.40e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491001101  36 HQKIVGY-KPTPLYALKSLAALFGvSTILVKDES-QRFGlnAFKMLGGAYAIAQLLcEKYHLdinafsfatfkssIKEKM 113
Cdd:PRK06608  14 HNRIKQYlHLTPIVHSESLNEMLG-HEIFFKVESlQKTG--AFKVRGVLNHLLELK-EQGKL-------------PDKIV 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491001101 114 TFATttdGNHGRGVAWAAQQLGQNAVIYMPKGSAQERVDAILRLGARCIVTEmnyddtvrftmqtARQNGWEVVQDTAWE 193
Cdd:PRK06608  77 AYST---GNHGQAVAYASKLFGIKTRIYLPLNTSKVKQQAALYYGGEVILTN-------------TRQEAEEKAKEDEEQ 140

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491001101 194 GYTKIPTW----IMQGYATLADEAVEQMAamgiARPTHVFLQAGVGAMAGG------VLGYLVDVFGArdlhsvivEPEL 263
Cdd:PRK06608 141 GFYYIHPSdsdsTIAGAGTLCYEALQQLG----FSPDAIFASCGGGGLISGtylakeLISPTSLLIGS--------EPLN 208

                        250       260
                 ....*....|....*....|....*...
gi 491001101 264 ADCLYRSGVKGQIVNVGGSMATIMAGLA 291
Cdd:PRK06608 209 ANDAYLSLKNNKIYRLNYSPNTIADGLK 236
L-Ser-dehyd cd06448
Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the ...
 45-319 1.50e-09

Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the conversion of L- , D-serine, or L-threonine to pyruvate/ketobutyrate and ammonia.


Pssm-ID: 107209  Cd Length: 316  Bit Score: 58.85  E-value: 1.50e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491001101  45 TPLYALKSLAALFGVSTILVKDESQRFGlnAFKMLG-GAyaiaqlLCEKYHLDINAFSFATFKSSikekmtfatttDGNH 123
Cdd:cd06448    2 TPLIESTALSKTAGCNVFLKLENLQPSG--SFKIRGiGH------LCQKSAKQGLNECVHVVCSS-----------GGNA 62

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491001101 124 GRGVAWAAQQLGQNAVIYMPKGSAQERVDAILRLGARCIVTEMNY---DDTVRFTMqTARQNGWEVVQ----DTAWEgyt 196
Cdd:cd06448   63 GLAAAYAARKLGVPCTIVVPESTKPRVVEKLRDEGATVVVHGKVWweaDNYLREEL-AENDPGPVYVHpfddPLIWE--- 138

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491001101 197 kiptwimqGYATLADEAVEQMAAMGiaRPTHVFLQAGVGAMAGGVLGYLVDVfGARDLHSVIVEPELADCLYRSGVKGQI 276
Cdd:cd06448  139 --------GHSSMVDEIAQQLQSQE--KVDAIVCSVGGGGLLNGIVQGLERN-GWGDIPVVAVETEGAHSLNASLKAGKL 207

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 491001101 277 V--NVGGSMATIMAGLACGEpNPLGWDILRNCATQFISCQDAVAA 319
Cdd:cd06448  208 VtlPKITSVATSLGAKTVSS-QALEYAQEHNIKSEVVSDRDAVQA 251
PRK12483 PRK12483
threonine dehydratase; Reviewed
 45-280 3.31e-09

threonine dehydratase; Reviewed


Pssm-ID: 237111 [Multi-domain]  Cd Length: 521  Bit Score: 58.66  E-value: 3.31e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491001101  45 TPLYALKSLAALFGVSTILVKDESQRfgLNAFKMLGGAYAIAQLLCEkyhldinafsfATFKSSIkekmtfaTTTDGNHG 124
Cdd:PRK12483  38 TPLQRAPNLSARLGNQVLLKREDLQP--VFSFKIRGAYNKMARLPAE-----------QLARGVI-------TASAGNHA 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491001101 125 RGVAWAAQQLGQNAVIYMPKGSAQERVDAILRLGARCIVTEMNYDDTVRFTMQTARQngwevvqdtawEGYTKIPTW--- 201
Cdd:PRK12483  98 QGVALAAARLGVKAVIVMPRTTPQLKVDGVRAHGGEVVLHGESFPDALAHALKLAEE-----------EGLTFVPPFddp 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491001101 202 -IMQGYATLADEAVEQMAAmgiarPTH-VFLQAGVGAMAGGVLGYLVDVfgaRDLHSVI-VEPELADCLYRSGVKGQIVN 278
Cdd:PRK12483 167 dVIAGQGTVAMEILRQHPG-----PLDaIFVPVGGGGLIAGIAAYVKYV---RPEIKVIgVEPDDSNCLQAALAAGERVV 238


                 ..
gi 491001101 279 VG 280
Cdd:PRK12483 239 LG 240
PRK08246 PRK08246
serine/threonine dehydratase;
121-305 3.76e-09

serine/threonine dehydratase;


Pssm-ID: 181319 [Multi-domain]  Cd Length: 310  Bit Score: 57.66  E-value: 3.76e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491001101 121 GNHGRGVAWAAQQLGQNAVIYMPKGSAQERVDAILRLGARCIVTEMNYDDTVRFTMQTARQNGweVVQDTAwegYTKIPT 200
Cdd:PRK08246  77 GNAGLAVAYAAAALGVPATVFVPETAPPAKVARLRALGAEVVVVGAEYADALEAAQAFAAETG--ALLCHA---YDQPEV 151

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491001101 201 WIMQGyaTLADEAVEQMAAmgiarPTHVFLQAGVGAMAGGVLGYlvdVFGARDLhsVIVEPELADCLYRSGVKGQIVNV- 279
Cdd:PRK08246 152 LAGAG--TLGLEIEEQAPG-----VDTVLVAVGGGGLIAGIAAW---FEGRARV--VAVEPEGAPTLHAALAAGEPVDVp 219

                        170       180
                 ....*....|....*....|....*..
gi 491001101 280 -GGSMATIMAGLACGEpnpLGWDILRN 305
Cdd:PRK08246 220 vSGIAADSLGARRVGE---IAFALARA 243
CBS_like cd01561
CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS ...
 45-262 8.61e-09

CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS is a unique heme-containing enzyme that catalyzes a pyridoxal 5'-phosphate (PLP)-dependent condensation of serine and homocysteine to give cystathionine. Deficiency of CBS leads to homocystinuria, an inherited disease of sulfur metabolism characterized by increased levels of the toxic metabolite homocysteine. Cysteine synthase on the other hand catalyzes the last step of cysteine biosynthesis. This subgroup also includes an O-Phosphoserine sulfhydrylase found in hyperthermophilic archaea which produces L-cysteine from sulfide and the more thermostable O-phospho-L-serine.


Pssm-ID: 107204 [Multi-domain]  Cd Length: 291  Bit Score: 56.37  E-value: 8.61e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491001101  45 TPLYALKSLAALFGVsTILVKDESQRFG-----LNAFKMLGGAYAiaqllcekyhldinafsfatfKSSIKEKMTFATTT 119
Cdd:cd01561    3 TPLVRLNRLSPGTGA-EIYAKLEFFNPGgsvkdRIALYMIEDAEK---------------------RGLLKPGTTIIEPT 60

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491001101 120 DGNHGRGVAWAAQQLGQNAVIYMPKGSAQERVDAILRLGARCI-VTEMNYDDtvrftMQTARQNGWEVVQDT--AWegyt 196
Cdd:cd01561   61 SGNTGIGLAMVAAAKGYRFIIVMPETMSEEKRKLLRALGAEVIlTPEAEADG-----MKGAIAKARELAAETpnAF---- 131

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491001101 197 kiptWIMQ---------GYATLADEAVEQMAamgiARPTHVFLQAGVGAMAGGVLGYLVDVFgaRDLHSVIVEPE 262
Cdd:cd01561  132 ----WLNQfenpanpeaHYETTAPEIWEQLD----GKVDAFVAGVGTGGTITGVARYLKEKN--PNVRIVGVDPV 196
CysK COG0031
Cysteine synthase [Amino acid transport and metabolism]; Cysteine synthase is part of the ...
 45-262 1.51e-08

Cysteine synthase [Amino acid transport and metabolism]; Cysteine synthase is part of the Pathway/BioSystem: Cysteine biosynthesis


Pssm-ID: 439802 [Multi-domain]  Cd Length: 301  Bit Score: 55.44  E-value: 1.51e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491001101  45 TPLYALKSLAALFGVsTILVKDESqrfgLN---------AFKMLggAYAIAQLLcekyhldinafsfatfkssIKEKMTF 115
Cdd:COG0031   14 TPLVRLNRLSPGPGA-EIYAKLES----FNpggsvkdriALSMI--EDAEKRGL-------------------LKPGGTI 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491001101 116 ATTTDGNHGRGVAWAAQQLGQNAVIYMPKGSAQERVDAILRLGARCIVTEMNYDdtvrftMQTARQNGWEVVQDTawEGY 195
Cdd:COG0031   68 VEATSGNTGIGLAMVAAAKGYRLILVMPETMSKERRALLRAYGAEVVLTPGAEG------MKGAIDKAEELAAET--PGA 139

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491001101 196 tkipTWIMQG---------YATLADEAVEQMAamgiARPTHVFLQAGVGAMAGGVLGYLVDVFgaRDLHSVIVEPE 262
Cdd:COG0031  140 ----FWPNQFenpanpeahYETTGPEIWEQTD----GKVDAFVAGVGTGGTITGVGRYLKERN--PDIKIVAVEPE 205
PRK08813 PRK08813
threonine dehydratase; Provisional
 121-184 1.71e-08

threonine dehydratase; Provisional


Pssm-ID: 236339 [Multi-domain]  Cd Length: 349  Bit Score: 55.79  E-value: 1.71e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491001101 121 GNHGRGVAWAAQQLGQNAVIYMPKGSAQERVDAILRLGARCIVTEMNYDDTVRFTMQTARQNGW 184
Cdd:PRK08813  90 GNHAQGVAWSAYRLGVQAITVMPHGAPQTKIAGVAHWGATVRQHGNSYDEAYAFARELADQNGY 153
PRK07048 PRK07048
threo-3-hydroxy-L-aspartate ammonia-lyase;
45-279 3.20e-08

threo-3-hydroxy-L-aspartate ammonia-lyase;


Pssm-ID: 235918 [Multi-domain]  Cd Length: 321  Bit Score: 54.64  E-value: 3.20e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491001101  45 TPLYALKSLAALFGvSTILVKDES-QRFGlnAFKMLGGAYAIAQLLCEKYHLDINAFSfatfkssikekmtfatttDGNH 123
Cdd:PRK07048  25 TPVLTSRTADARTG-AQVFFKCENfQRMG--AFKFRGAYNALSQFSPEQRRAGVVTFS------------------SGNH 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491001101 124 GRGVAWAAQQLGQNAVIYMPKGSAQERVDAILRLGARCIVtemnYDdtvRFTmqTARQngwEVVQDTAWE-GYTKIPTW- 201
Cdd:PRK07048  84 AQAIALSARLLGIPATIVMPQDAPAAKVAATRGYGGEVVT----YD---RYT--EDRE---EIGRRLAEErGLTLIPPYd 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491001101 202 ---IMQGYATLADEAVEQMAAMGIarpthVFLQAGVG------AMAGGVLGYLVDVFGardlhsviVEPELADCLYRSGV 272
Cdd:PRK07048 152 hphVIAGQGTAAKELFEEVGPLDA-----LFVCLGGGgllsgcALAARALSPGCKVYG--------VEPEAGNDGQQSFR 218


                 ....*..
gi 491001101 273 KGQIVNV 279
Cdd:PRK07048 219 SGEIVHI 225
PRK07334 PRK07334
threonine dehydratase; Provisional
 121-305 4.95e-08

threonine dehydratase; Provisional


Pssm-ID: 235994 [Multi-domain]  Cd Length: 403  Bit Score: 54.51  E-value: 4.95e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491001101 121 GNHGRGVAWAAQQLGQNAVIYMPKGSAQERVDAILRLGARCIVTEMNYDDtvrftmqtARQNGWEVVQDtawEGYTKI-P 199
Cdd:PRK07334  80 GNHAQGVAYHAQRLGIPATIVMPRFTPTVKVERTRGFGAEVVLHGETLDE--------ARAHARELAEE---EGLTFVhP 148

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491001101 200 ---TWIMQGYATLADEAVEqmaamgiARPThvfLQAGVGAMAGGVL--GYLVDVFGAR-DLHSVIVEPELADCLYrSGVK 273
Cdd:PRK07334 149 yddPAVIAGQGTVALEMLE-------DAPD---LDTLVVPIGGGGLisGMATAAKALKpDIEIIGVQTELYPSMY-AAIK 217

                        170       180       190
                 ....*....|....*....|....*....|..
gi 491001101 274 GQIVNVGGSmaTIMAGLACGEPNPLGWDILRN 305
Cdd:PRK07334 218 GVALPCGGS--TIAEGIAVKQPGQLTLEIVRR 247
PRK08638 PRK08638
bifunctional threonine ammonia-lyase/L-serine ammonia-lyase TdcB;
117-217 2.96e-06

bifunctional threonine ammonia-lyase/L-serine ammonia-lyase TdcB;


Pssm-ID: 236317 [Multi-domain]  Cd Length: 333  Bit Score: 48.58  E-value: 2.96e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491001101 117 TTTDGNHGRGVAWAAQQLGQNAVIYMPKGSAQERVDAILRLGARCIVTEMNYDDTVRFTMQTARQngwevvqdtawEGYT 196
Cdd:PRK08638  80 ACSAGNHAQGVALSCALLGIDGKVVMPKGAPKSKVAATCGYGAEVVLHGDNFNDTIAKVEEIVEE-----------EGRT 148

                         90       100
                 ....*....|....*....|....*
gi 491001101 197 KIPTW----IMQGYATLADEAVEQM 217
Cdd:PRK08638 149 FIPPYddpkVIAGQGTIGLEILEDL 173
PRK05638 PRK05638
threonine synthase; Validated
 115-263 1.95e-05

threonine synthase; Validated


Pssm-ID: 235539 [Multi-domain]  Cd Length: 442  Bit Score: 46.34  E-value: 1.95e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491001101 115 FATTTDGNHGRGVAWAAQQLGQNAVIYMPKGSAQERVDAILRLGARCIVTEMNYDDTVRFTMQTARQNGWevvqdtaweg 194
Cdd:PRK05638 115 FIVASDGNAAASVAAYSARAGKEAFVVVPRKVDKGKLIQMIAFGAKIIRYGESVDEAIEYAEELARLNGL---------- 184

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491001101 195 YTKIPTW---IMQGYATLADEAVEQMAamgiarPTHVFLQAGVGAmaggvlgYLVDVF-GARDLHSVIVEPEL 263
Cdd:PRK05638 185 YNVTPEYniiGLEGQKTIAFELWEEIN------PTHVIVPTGSGS-------YLYSIYkGFKELLEIGVIEEI 244
ThrC COG0498
Threonine synthase [Amino acid transport and metabolism]; Threonine synthase is part of the ...
 45-255 1.15e-04

Threonine synthase [Amino acid transport and metabolism]; Threonine synthase is part of the Pathway/BioSystem: Threonine biosynthesis


Pssm-ID: 440264 [Multi-domain]  Cd Length: 394  Bit Score: 44.04  E-value: 1.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491001101  45 TPLYALKSLAALFGvSTILVKDEsqrfGLN---AFKMLGgayaiAQLLCEKyhldinafsfatfkssIKE--KMTFATTT 119
Cdd:COG0498   67 TPLVKAPRLADELG-KNLYVKEE----GHNptgSFKDRA-----MQVAVSL----------------ALErgAKTIVCAS 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491001101 120 DGNHGRGVAWAAQQLGQNAVIYMPKGS-AQERVDAILRLGARCIVTEMNYDDTVRFTMQTARQNGWEVVQDTAWegytki 198
Cdd:COG0498  121 SGNGSAALAAYAARAGIEVFVFVPEGKvSPGQLAQMLTYGAHVIAVDGNFDDAQRLVKELAADEGLYAVNSINP------ 194

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 491001101 199 ptWIMQGYATLADEAVEQMAAMgiarPTHVFLqaGVGAmAGGVLGYLVdvfGARDLH 255
Cdd:COG0498  195 --ARLEGQKTYAFEIAEQLGRV----PDWVVV--PTGN-GGNILAGYK---AFKELK 239
D-Ser-dehyd cd06447
D-Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the ...
 121-305 3.62e-04

D-Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the conversion of L- or D-serine to pyruvate and ammonia. D-serine dehydratase serves as a detoxifying enzyme in most E. coli strains where D-serine is a competitive antagonist of beta-alanine in the biosynthetic pathway to pentothenate and coenzyme A. D-serine dehydratase is different from other pyridoxal-5'-phosphate-dependent enzymes in that it catalyzes alpha, beta-elimination reactions on amino acids.


Pssm-ID: 107208  Cd Length: 404  Bit Score: 42.33  E-value: 3.62e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491001101 121 GNHGRGVAWAAQQLGQNAVIYMPKGSAQERVDAILRLGARCIVTEMNYDDTV-RFTMQTARQNGWEVVQDtawEGYTKIp 199
Cdd:cd06447  143 GNLGLSIGIMAAALGFKVTVHMSADAKQWKKDKLRSKGVTVVEYETDYSKAVeEGRKQAAADPMCYFVDD---ENSRDL- 218

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491001101 200 twiMQGYATLADEAVEQMAAMGI----ARPTHVFLQAGVGAMAGGVLGYLVDVFGArDLHSVIVEPELADCL---YRSGV 272
Cdd:cd06447  219 ---FLGYAVAASRLKAQLAELGIkvdaEHPLFVYLPCGVGGAPGGVAFGLKLIFGD-NVHCFFAEPTHSPCMllgMATGL 294

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 491001101 273 KGQI--VNVGGSMATIMAGLACGEPNPLGWDILRN 305
Cdd:cd06447  295 HDKIsvQDIGIDNRTAADGLAVGRPSGLVGKLMEP 329
PRK10717 PRK10717
cysteine synthase A; Provisional
 45-165 3.09e-03

cysteine synthase A; Provisional


Pssm-ID: 182672 [Multi-domain]  Cd Length: 330  Bit Score: 39.46  E-value: 3.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491001101  45 TPLYALKSLAALFGvSTILVKDESQRFGlNAFKMLGGAYAIaqllcekyhLDinafsfATFKSSIKEKMTFATTTDGNHG 124
Cdd:PRK10717  14 TPLIRLNRASEATG-CEILGKAEFLNPG-GSVKDRAALNII---------WD------AEKRGLLKPGGTIVEGTAGNTG 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 491001101 125 RGVAWAAQQLGQNAVIYMPKGSAQERVDAILRLGARCIVTE 165
Cdd:PRK10717  77 IGLALVAAARGYKTVIVMPETQSQEKKDLLRALGAELVLVP 117
PRK02991 PRK02991
D-serine dehydratase; Provisional
 205-266 5.70e-03

D-serine dehydratase; Provisional


Pssm-ID: 235096  Cd Length: 441  Bit Score: 38.71  E-value: 5.70e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491001101 205 GYATLADEAVEQMAAMGIA----RPTHVFLQAGVGAMAGGVLGYLVDVFGArDLHSVIVEPELADC 266
Cdd:PRK02991 244 GYAVAGLRLKAQLAEQGIVvdadHPLFVYLPCGVGGGPGGVAFGLKLAFGD-HVHCFFAEPTHSPC 308
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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